Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin

Article Abstract:

Experiment was conducted to examine the substrate binding domain of the alpha subunit of the Thermoplasma acidophilum thermosome, the archaeal group II chaperonin, by solving its crystal structure at 2.3 angstrom resolution. Two datasets, which represent the two extremes of distribution in unit cell size were collected from single crystals, one at 2.8 angstrom on a rotating anode X-ray generator, the other at 2.3 angstrom with synchrotron radiation. The holochaperonin models indicate a dual role of this helical protrusion in substrate binding and controlling access to the central cavity.

Protein folding, Plant growing media

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Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid

Article Abstract:

X-ray diffraction analysis of the complex formed by the inosine-5'-monophosphate dehydrogenase (IMPDH), IMP and mycophenolic acid (MPA) shows IMPDH having a core- and flanking-domain, with the core domain carrying the active site. IMP was shown to inhibit IMPDH activity by replacing the nicotinamide portion of the nicotinamide adenine dinucleotide cofactor.

Immunosuppressive agents

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A unique RNA fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function

Article Abstract:

The x-ray crystal structure of RumA/RNA/S-adenosylhomocysteine (SAH) ternary complex, which is the first RNA bound structure of a ribosomal RNA-modifying enzyme and of an RNA methyltransferase, is described. The unique quaternary interaction in the enzyme-RNA complex uncovers a mechanism for achieving unique selectivity.

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